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Covalent Immobilization of Candida rugosa Lipase at Alkaline pH and Their Application in the Regioselective Deprotection of Per-O-acetylated Thymidine

AuthorsRivero, Cintia W.; Palomo, José Miguel
Issue Date2-Aug-2016
PublisherMultidisciplinary Digital Publishing Institute
CitationCatalysts 6(8): 115 (2016)
AbstractLipase from <i>Candida rugosa</i> (CRL) was stabilized at alkaline pH to overcome the inactivation problem and was immobilized for the first time by multipoint covalent attachment on different aldehyde-activated matrices. PEG was used as a stabilizing agent on the activity of CRL. At these conditions, CRL maintained 50% activity at pH 10 after 17 h incubation in the presence of 40% (<i>w</i>/<i>v</i>) of PEG, whereas the enzyme without additive was instantaneously inactive after incubation at pH 10. Thus, this enzyme was covalently immobilized at alkaline pH on three aldehyde-activated supports: aldehyde-activated Sepharose, aldehyde-activated Lewatit105 and heterofunctional aldehyde-activated EDA-Sepharose in high overall yields. Heterogeneous stable CRL catalysts at high temperature and solvent were obtained. The aldehyde-activated Sepharose-CRL preparation maintained 70% activity at 50 °C or 30% (<i>v</i>/<i>v</i>) acetonitrile after 22 h and exhibited high regioselectivity in the deprotection process of per-<i>O</i>-acetylated thymidine, producing the 3′-OH-5′-OAc-thymidine in 91% yield at pH 5.
Identifiersdoi: 10.3390/catal6080115
Appears in Collections:(ICP) Artículos
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